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Search results

1000 results found for “myelin basic protein”

Name

Description

Product #

Price

Quantity

Shipping Method

  • View Data Sheet

    Name :

    DNAL4 Human

    Description:

    Dynein Axonemal Light Chain 4 Human Recombinant

    Dynein light chain 4 axonemal, DNAL4, PIG27.

    Product # :

    PRO-227

    Price :

    Quantity :

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    Description

    DNAL4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-105 a.a) and having a molecular mass of 14.1kDa.DNAL4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DNAL4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      DNAL4 is a member of the dynein light chain family. DNAL4 is a component of the dynein motor complex in cells that converts the chemical energy contained in ATP into the mechanical energy of movement. Dynein transports various cellular cargos by moving the length of cytoskeletal microtubules towards the minus-end of the microtubule, which is typically oriented towards the cell center.

    • Synonyms

      Dynein light chain 4 axonemal, DNAL4, PIG27.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGETEGKKDE ADYKRLQTFP LVRHSDMPEE MRVETMELCV TACEKFSNNN ESAAKMIKET MDKKFGSSWH VVIGEGFGFE ITHEVKNLLY LYFGGTLAVC VWKCS.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Dnal4 Human
  • View Data Sheet

    Name :

    Cys-Protein-G

    Description:

    Cys-Protein G Recombinant

    Product # :

    PRO-1238

    Price :

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    Description

    Cys-Protein G Recombinant produced in E.Coli, is a single non-glycosylated polypeptide chain containing 201 amino acids and having a cys on N-terminal. Cys-Protein G has a predicted molecular mass of approximately 21.9kDa but it migrates with an apparent molecular mass of 40kDa in SDS-PAGE. The Cys-Protein G is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized without any additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein G should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Protein G in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CLPKTDTYKL ILNGKTLKGE TTTEAVDAAT AEKVFKQYAN DNGVDGEWTY DDATKTFTVT EKPEVIDASE LTPAVTTYKL VINGKTLKGE TTTEAVDAAT AEKVFKQYAN DNGVDGEWTY DDATKTFTVT EKPEVIDASE LTPAVTTYKL VINGKTLKGE TTTKAVDAET AEKAFKQYAN DNGVDGVWTY DDATKTFTVT E.

    • Specificity

      The recombinant Protein G is a genetically engineered protein contains 3 IgG-binding regions of protein G.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cys Protein G His
  • View Data Sheet

    Name :

    SNCA E46K, Human

    Description:

    Alpha-Synuclein E46K Human Recombinant

    SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.

    Product # :

    PRO-2626

    Price :

    Quantity :

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    Description

    SNCA E46K Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-140a.a.) and having a molecular mass of 14.4kDa.SNCA is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SNCA protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 7.5) and 0.1 M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNCA or Alpha-synuclein is a protein with undisclosed function that mainly concentrated in the brain tissue, mainly in the tips of the neurons in the presynaptic terminals. Almost 1% of the proteins in the brain tissues are synucleins. The protein is located mainly in the hippocampus, thalamus, cerebellum & neocortex. Smaller amounts of the SNCA protein can be found in the neuroglial cells. The MITF protein regulates the SNCA expression in melanocytic cells.

    • Synonyms

      SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKKGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Synuclein Alpha
  • View Data Sheet

    Name :

    MYL2 Human

    Description:

    Myosin Light Chain 2 Human Recombinant

    MLC2, CMH10, MYL-2, Myosin regulatory light chain 2, MYOSIN LIGHT CHAIN REGULATORY VENTRICULAR, DKFZp779C0562, MYL2, MLC-2v, MLC-2.

    Product # :

    PRO-524

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    MYL2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 186 amino acids (1-166) and having a molecular mass of 20.9 kDa. MYL2 is fused to a 20 amino acid His Tag fused at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MYL2 solution containing 20mM Tris pH-8, 40% glycerol and 5mM CaCl2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MYL2 regulatory light chain is associated with cardiac myosin beta (or slow) heavy chain. Ca+ activates the phosphorylation of regulatory light chain that in turn activates contraction. Mutations in this MYL2 gene are related with mid-left ventricular chamber type hypertrophic cardiomyopathy. MYL2 is an essential protein that plays a role in the regulation of myosin ATPase activity in smooth muscle. MYL2 phosphorylation is regulated by ROCK and MLC kinase and is involved in platelet biogenesis by controlling proplatelet formation and fragmentation.

    • Synonyms

      MLC2, CMH10, MYL-2, Myosin regulatory light chain 2, MYOSIN LIGHT CHAIN REGULATORY VENTRICULAR, DKFZp779C0562, MYL2, MLC-2v, MLC-2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAPKKAKKRA GGANSNVFSM FEQTQIQEFK EAFTIMDQNR DGFIDKNDLR DTFAALGRVN VKNEEIDEMI KEAPGPINFT VFLTMFGEKL KGADPEETIL NAFKVFDPEG KGVLKADYVR EMLTTQAERF SKEEVDQMFA AFPPDVTGNL DYKNLVHIIT HGEEKD.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Myl2 Human
  • View Data Sheet

    Name :

    TPT1 Mouse

    Description:

    Tumor Protein Translationally-Controlled 1 Mouse Recombinant

    Translationally-controlled tumor protein, TCTP, 21 kDa polypeptide, p21, p23.

    Product # :

    PRO-2196

    Price :

    Quantity :

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    • description
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    • formulation
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    • More Info

    Description

    TPT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (1-172 a.a) and having a molecular mass of 22.1kDa.TPT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TPT1 protein solution (1mg/ml) containing Phosphate Buffered Saline, 10% glycerol And 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TPT1 takes part in calcium binding and microtubule stabilization. TPT1 is an immunoglobulin E dependent histamine-releasing factor produced by lymphocytes of atopic children and present in biologic fluids of allergic patients. TPT1 protein is similar to p23, a protein of Ehrlich ascites tumor cells, synthesized in the exponentially growing tumor. TPT1 is similar with IgE-dependent histamine releasing factor. TPT1 has a cell housekeeping function. TPT1 is involved in spermatogenesis and acts as a calcium binding protein of the human placenta that regulates calcium handling in trophoblast cells.

    • Synonyms

      Translationally-controlled tumor protein, TCTP, 21 kDa polypeptide, p21, p23.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMMIIYR DLISHDELFS DIYKIREIAD GLCLEVEGKM VSRTEGAIDD SLIGGNASAE GPEGEGTEST VVTGVDIVMN HHLQETSFTK EAYKKYIKDY MKSLKGKLEE QKPERVKPFM TGAAEQIKHI LANFNNYQFF IGENMNPDGM VALLDYREDG VTPFMIFFKD GLEMEKC.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tpt1 Mouse
  • View Data Sheet

    Name :

    HAPLN1 Human, HEK

    Description:

    Hyaluronan And Proteoglycan Link Protein 1 Human Recombinant, HEK

    Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.

    Product # :

    PRO-2776

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    Description

    HAPLN1 Human Recombinant produced in HEK293 Cells.is a single, glycosylated polypeptide chain containing 345 amino acids (16-354 a.a.) and having a molecular mass of 39.3kDa. HAPLN1 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    HAPLN1 protein solution (0.25mg/ml) containing 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range is ≤ 1 ug/ml and is measured by its binding ability in a functional ELISA with Hyaluronic acid.

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    • Synonyms

      Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      DHLSDNYTLD HDRAIHIQAE NGPHLLVEAE QAKVFSHRGG NVTLPCKFYR DPTAFGSGIH KIRIKWTKLT SDYLKEVDVF VSMGYHKKTY GGYQGRVFLK GGSDSDASLV ITDLTLEDYG RYKCEVIEGL EDDTVVVALD LQGVVFPYFP RLGRYNLNFH EAQQACLDQD AVIASFDQLY DAWRGGLDWC NAGWLSDGSV QYPITKPREP CGGQNTVPGV RNYGFWDKDK SRYDVFCFTS NFNGRFYYLI HPTKLTYDEA VQACLNDGAQ IAKVGQIFAA WKILGYDRCD AGWLADGSVR YPISRPRRRC SPTEAAVRFV GFPDKKHKLY GVYCFRAYNH HHHHH.

    • Background

      Bibliography:

      Armingol, E., Officer, A., Harismendy, O., & Lewis, N. E. (2020). Deciphering cell-cell interactions and communication from gene expression. Nature Reviews Genetics, 21(2), 71-88.

      Bonnans, C., Chou, J., & Werb, Z. (2014). Remodelling the extracellular matrix in development and disease. Nature Reviews Molecular Cell Biology, 15(12), 786-801.

      Bönnemann, C. G. (2011). The collagen VI-related myopathies: muscle meets its matrix. Nature Reviews Neurology, 7(7), 379-390.

      Choi, H., Lee, R. H., Bazhanov, N., Oh, J. Y., & Prockop, D. J. (2011). Anti-inflammatory protein TSG-6 secreted by activated MSCs attenuates zymosan-induced mouse peritonitis by decreasing TLR2/NF-κB signaling in resident macrophages. Blood, 118(2), 330-338.

      Lesley, J., Hyman, R., & Kincade, P. W. (1993). CD44 and its interaction with extracellularmatrix. Advances in Immunology, 54, 271-335.

      Sherman, L. S., Rizvi, T. A., Karyala, S., & Ratner, N. (2000). CD44 enhances neuregulin signaling by Schwann cells. The Journal of Cell Biology, 150(5), 1071-1084.

      Toole, B. P. (2004). Hyaluronan: from extracellular glue to pericellular cue. Nature Reviews Cancer, 4(7), 528-539.

      Yamada, Y., Itano, N., Narimatsu, H., Kudo, T., Morozumi, K., Hirohashi, S., ... & Kimata, K. (2004). Elevated transcript level of hyaluronan synthase1 gene correlates with poor prognosis of human colon cancer. Clinical & Experimental Metastasis, 21(1), 57-63.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Hapln1 Human Hek
  • View Data Sheet

    Name :

    SNCA A30P/A53T Human

    Description:

    Alpha Synuclein A30P/A53T Human Recombinant

    Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    Product # :

    PRO-160

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    Description

    A-Synuclein A30P/A53T Human Recombinant which is a Parkinson’s disease-related double mutant, produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.5kDa (molecular size on SDS-PAGE will appear higher). The Recombinant Human a-Synuclein A30P/A53T is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNCA A30P/A53T protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

    • Synonyms

      Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAP GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.

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    Snca A30P A53T Human
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    Name :

    b NGF Mouse

    Description:

    Beta-Nerve Growth Factor Mouse

    Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    Product # :

    CYT-440

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    Description

    NGF beta Mouse produced in Submaxillary Gland of Grown Mouse is a homodimer, non-glycosylated, polypeptide chain containing 2 identical 120 amino acids and having a molecular mass of 13,471 Dalton each.The NGF beta Mouse is purified by advanced biology purification technology.

    Source

    Submaxillary Gland of Grown Mouse.

    Formulation

    The NGF beta Mouse was lyophilized from solution containing 5% mannitol and 1% HSA.

    Purity

    Greater than 98% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE .

    Biological Activity

    The method used to test the bioassay is the NGF-dependent survival of dorsal root ganglia neurons of chick embryo, corresponding to a Specific Activity of 500,000IU/mg.

    More Info

    • Introduction

      NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.

    • Synonyms

      Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Mouse Beta-NGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Murine NGF-Beta should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Murine NGF-beta in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SSTHPVFHMGEF SVCDSVSVWV GDKTTATDIK GKEVTVLAEV NINNSVFRQY FFETKCRASN PVESGCRGID SKHWNSYCTT THTFVKALTT DEKQAAWRFI RIDTACVCVL SRKATRRG.

    • Background

      What is the molecular weight/Mw of B NGF Protein?
      B NGF Protein has a total Mw of 13kDa.

      What is the source or expression system of B NGF Protein?
      Submaxillary Gland of Grown Mouse.

      What is the Purity of B NGF Protein?

      B NGF Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of B NGF Protein?
      The method used to test the bioassay is the NGF-dependent survival of dorsal root ganglia neurons of chick embryo, corresponding to a Specific Activity of 500,000IU/mg.

      What is the amino acid sequence of B NGF Protein?
      SSTHPVFHMGEF SVCDSVSVWV GDKTTATDIK GKEVTVLAEV NINNSVFRQY FFETKCRASN PVESGCRGID SKHWNSYCTT THTFVKALTT DEKQAAWRFI RIDTACVCVL SRKATRRG.

      What applications can B NGF Protein be used in?
      B NGF Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for XXX Protein?
      The endotoxin level is minimal, XXX Protein was purified using conventional chromatography techniques.

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    Beta Ngf Mouse
  • View Data Sheet

    Name :

    APOB Protein

    Description:

    Apolipoprotein-B Human Recombinant

    APOB, APO-B, Apolipoprotein B.

    Product # :

    CYT-1233

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    Description

    The APOBHuman is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The APOBHis-Tagged Fusion Protein, produced in E. coli, is a 31kDa protein containing 201 amino acid residues of the APOBHuman, 1406-1606 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 80% as determined by SDS-PAGE.

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    • Synonyms

      APOB, APO-B, Apolipoprotein B.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized APOBat -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      Apolipoprotein-B (ApoB) is the main apolipoprotein of LDL, VLDL, IDL and chylomicrons particles which serves as the carrier of lipids in the water surrounding the cells in every tissue across the body. Apolipoprotein B acts as the key organizing protein of all other carriers of lipids. across LDL membranes, ApoB also plays a role as a ligand for LDL receptors in many cells across the body, meaning, it shows that lipid carriers that are set to cross into cells with Apolipoprotein B receptors, this is how lipids are transported within and into cells.

      What is the molecular weight/Mw of APOB Protein?
      APOB Protein has a total Mw of 31kDa.

      What is the source or expression system of APOB Protein?
      Escherichia Coli.

      What is the Purity of APOB Protein?
      APOB Protein is >80% pure as determined by SDS-PAGE.

      What is the Biological Activity of APOB Protein?
      The biological functionality of APOB Protein will be determined in the future.

      What is the amino acid sequence of APOB Protein?
      APOB Protein is composed from 201 amino acids.

      What applications can APOB Protein be used in?
      APOB Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for APOB Protein?
      The endotoxin level is minimal, APOB Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Human Apob
  • View Data Sheet

    Name :

    NCAM1 Human

    Description:

    Neural Cell Adhesion Molecule 1 Human Recombinant

    Neural cell adhesion molecule 1, Neural cell adhesion molecule 1 isoform3, N-CAM-1, NCAM-1, CD56, NCAM1, NCAM, MSK39

    Product # :

    PRO-2710

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    Description

    NCAM1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 593 amino acids (20-603 a.a) and having a molecular mass of 65.7kDa.NCAM1 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The NCAM1 solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neural Cell Adhesion Molecule 1 (NCAM1) is apart of the immunoglobulin superfamily. NCAM1 bindsspecifically to neurite fasciculation, neuronneuron adhesion, outgrowth of neurites, and more. The polysialyation of NCAM1 reduces its adhesive property and increases its neurite outgrowth promoting features.NCAM1is mainly expressed in NK cells and a subset of T lymphocytes that mediate MHC-unrestricted cellmediated cytotoxicity. High expression of NCAM-1 differentiates NK cells as having an activated phenotype. During hematopoiesis, NCAM1plays a role as the prototypic marker of NK cells and also present on subset of CD4+, CD8+ and T cells. In cell adhesion, NCAM1 contributes to cell-cell adhesion during embryonic development.

    • Synonyms

      Neural cell adhesion molecule 1, Neural cell adhesion molecule 1 isoform3, N-CAM-1, NCAM-1, CD56, NCAM1, NCAM, MSK39

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPLQVDIVP SQGEISVGES KFFLCQVAGD AKDKDISWFS PNGEKLTPNQ QRISVVWNDD SSSTLTIYNA NIDDAGIYKC VVTGEDGSES EATVNVKIFQ KLMFKNAPTP QEFREGEDAV IVCDVVSSLP PTIIWKHKGR DVILKKDVRF IVLSNNYLQI RGIKKTDEGT YRCEGRILAR GEINFKDIQV IVNVPPTIQA RQNIVNATAN LGQSVTLVCD AEGFPEPTMS WTKDGEQIEQ EEDDEKYIFS DDSSQLTIKK VDKNDEAEYI CIAENKAGEQ DATIHLKVFA KPKITYVENQ TAMELEEQVT LTCEASGDPI PSITWRTSTR NISSEEKTLD GHMVVRSHAR VSSLTLKSIQ YTDAGEYICT ASNTIGQDSQ SMYLEVQYAP KLQGPVAVYT WEGNQVNITC EVFAYPSATI SWFRDGQLLP SSNYSNIKIY NTPSASYLEV TPDSENDFGN YNCTAVNRIG QESLEFILVQ ADTPSSPSID QVEPYSSTAQ VQFDEPEATG GVPILKYKAE WRAVGEEVWH SKWYDAKEAS MEGIVTIVGL KPETTYAVRL AALNGKGLGE ISAASEFKTQ PVHSPPPHHH HHH

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    Ncam1 Human
  • View Data Sheet

    Name :

    LIN7C Human

    Description:

    LIN7C Human Recombinant

    LIN-7-C, LIN-7C, MALS-3, MALS3, VELI3, Lin-7 homolog C, Protein lin-7 homolog C, Mammalian lin-seven protein 3, MALS-3, Veli-3, LIN7C, Vertebrate lin-7 homolog 3.

    Product # :

    PRO-1305

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    Description

    LIN7C Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197 a.a.) and having a molecular mass of 24.2 kDa. LIN7C is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LIN7C protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE

    More Info

    • Introduction

      LIN7C has a part in establishing and preserving the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. LIN7C forms membrane-associated multiprotein complexes which regulate distribution and recycling of proteins to the appropriate membrane domains.

    • Synonyms

      LIN-7-C, LIN-7C, MALS-3, MALS3, VELI3, Lin-7 homolog C, Protein lin-7 homolog C, Mammalian lin-seven protein 3, MALS-3, Veli-3, LIN7C, Vertebrate lin-7 homolog 3.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGCSHHHHHH SSGLVPRGSH MGSMAALGEP VRLERDICRA IELLEKLQRS GEVPPQKLQA LQRVLQSEFC NAVREVYEHV YETVDISSSP EVRANATAKA TVAAFAASEG HSHPRVVELP KTEEGLGFNI MGGKEQNSPI YISRIIPGGI ADRHGGLKRG DQLLSVNGVS VEGEHHEKAV ELLKAAQGKV KLVVRYTPKV LEEMESRFEK MRSAKRRQQT.

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    Lin7C Human
  • View Data Sheet

    Name :

    CST3 Protein, His

    Description:

    Cystatin-C Human Recombinant, His Tag

    Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    Product # :

    PRO-656

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    Description

    Cystatin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 129 amino acids and having a molecular mass of 14.5 kDa. The protein contains an extra His tag at N-terminus. The Cystatin-C amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q6FGW9 amino acids 28–146.The Cystatin-C is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS PAGE.

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    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cystatin C Human Recombinant
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    Name :

    S100A8 Human, His-Myc

    Description:

    S100 Calcium Binding Protein A8, His-Myc Tag Human Recombinant

    S100 Calcium Binding Protein A8, S100 Calcium-Binding Protein A8 (Calgranulin A), Migration Inhibitory Factor-Related Protein 8, Leukocyte L1 Complex Light Chain , Urinary Stone Protein Band A, Calprotectin L1L Subunit, Cystic Fibrosis Antigen, Calgranulin-A, MRP8, CAGA, CFAG, P8, S100 Calcium Binding Protein A8 (Calgranulin A), S100 Calcium-Binding Protein A8, Calgranulin A, 60B8AG, CP-10, MA38, MRP-8, CGLA, L1Ag, MIF, NIF.

    Product # :

    PRO-2329

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    Description

    S100A8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 127 amino acids (1-93) and having a molecular mass of 14.5kDa. S100A8 is fused to a 24 aa His-tag at N-terminus and to a 10 aa Myc-tag at C-terminus.

    Source

    Escherichia Coli.

    Formulation

    The S100A8 solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

    • Synonyms

      S100 Calcium Binding Protein A8, S100 Calcium-Binding Protein A8 (Calgranulin A), Migration Inhibitory Factor-Related Protein 8, Leukocyte L1 Complex Light Chain , Urinary Stone Protein Band A, Calprotectin L1L Subunit, Cystic Fibrosis Antigen, Calgranulin-A, MRP8, CAGA, CFAG, P8, S100 Calcium Binding Protein A8 (Calgranulin A), S100 Calcium-Binding Protein A8, Calgranulin A, 60B8AG, CP-10, MA38, MRP-8, CGLA, L1Ag, MIF, NIF.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMLTELE KALNSIIDVY HKYSLIKGNF HAVYRDDLKK LLETECPQYI RKKGADVWFK ELDINTDGAV NFQEFLILVI KMGVAAHKKS HEESHKEEQK LISEEDL.

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    S100A8 His Myc Human
  • View Data Sheet

    Name :

    GMFB Mouse

    Description:

    Glia Maturation Factor Beta Mouse Recombinant

    Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.

    Product # :

    CYT-006

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    Description

    Glia Maturation Factor-Beta (GMF-Beta) Mouse Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.6kDa. GMF-Beta, Mouse Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GMF-beta protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      GMFB is part of the GMF subfamily of the larger actin-binding protein ADF family. GMFB is phosphorylated after phorbol ester stimulation, and is crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.

    • Synonyms

      Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GMF-B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMF-beta should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized GMFB in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
      VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
      MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.

    • Background

      What is the molecular weight/Mw of GMFB MOUSE Protein?
      GMFB MOUSE Protein has a total Mw of 16.6kDa.

      What is the source or expression system of GMFB MOUSE Protein?
      Escherichia Coli.

      What is the Purity of GMFB MOUSE Protein?
      GMFB MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of GMFB MOUSE Protein?
      The biological functionality of GMFB MOUSE Protein will be determined in the future.

      What is the amino acid sequence of GMFB MOUSE Protein?
      SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
      VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
      MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.

      What applications can GMFB MOUSE Protein be used in?
      GMFB MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GMFB MOUSE Protein?
      The endotoxin level is minimal, GMFB MOUSE Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Gmfb Mouse
  • View Data Sheet

    Name :

    MMP 7 Human

    Description:

    Matrix Metalloproteinase-7 Human Recombinant

    Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7.

    Product # :

    ENZ-867

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    Description

    MMP-7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (95-267 a.a) and having a molecular mass of 19.2kDa.MMP7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MMP7 protein solution (1mg/ml) containing 20mM Tris 8.0 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.

    • Synonyms

      Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MYSLFPNSPK WTSKVVTYRI VSYTRDLPHI TVDRLVSKAL NMWGKEIPLH FRKVVWGTAD IMIGFARGAH GDSYPFDGPG NTLAHAFAPG TGLGGDAHFD EDERWTDGSS LGINFLYAAT HELGHSLGMG HSSDPNAVMY PTYGNGDPQN FKLSQDDIKG IQKLYGKRSN SRKK.

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    Mmp 7 Human
  • View Data Sheet

    Name :

    HNRNPK Human

    Description:

    Heterogeneous Nuclear Ribonucleoprotein K Human Recombinant

    CSBP, HNRPK, TUNP, Heterogeneous nuclear ribonucleoprotein K, hnRNP K, Transformation up-regulated nuclear protein, HNRNPK.

    Product # :

    PRO-1539

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    Description

    HNRNPK Human Recombinant produced in E. coli is a single polypeptide chain containing 299 amino acids (1-276) and having a molecular mass of 33kDa. HNRNPK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HNRNPK solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Heterogeneous Nuclear Ribonucleoprotein K, also known as HNRNPK, is a part of the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). HNRNPK takes part in p53/TP53 reaction to DNA damage, acting at the level of both transcription activation and repression. HNRNPK is located in the nucleoplasm and has 3 repeats of KH domains which bind to RNAs.

    • Synonyms

      CSBP, HNRPK, TUNP, Heterogeneous nuclear ribonucleoprotein K, hnRNP K, Transformation up-regulated nuclear protein, HNRNPK.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMETEQPE ETFPNTETNG EFGKRPAEDM EEEQAFKRSR NTDEMVELRI LLQSKNAGAV IGKGGKNIKA LRTDYNASVS VPDSSGPERI LSISADIETI GEILKKIIPT LEEGLQLPSP TATSQLPLES DAVECLNYQH YKGSDFDCEL RLLIHQSLAG GIIGVKGAKI KELRENTQTT IKLFQECCPH STDRVVLIGG KPDRVVECIK IILDLISESP IKGRAQPYDP NFYDETYDYG GFTMMFDDRR GRPVGFPMRG RGGFDRMPPG RGGRPMPPS.

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    Hnrnpk Human
  • View Data Sheet

    Name :

    MRTO4 Human

    Description:

    mRNA Turnover 4 Human Recombinant

    MRNA Turnover 4 Homolog (S. Cerevisiae), MRT4 MRNA Turnover 4 Homolog (S. Cerevisiae), 60S Acidic Ribosomal Protein PO, Chromosome 1 Open Reading Frame 33, C1orf33, MRT4, DJ657E11.4.

    Product # :

    PRO-1233

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    Description

    MRTO4 Human Recombinant produced in E. coli is a single polypeptide chain containing 262 amino acids (1-239) and having a molecular mass of 29.9 kDa.MRTO4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MRTO4 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      mRNA turnover protein 4 homolog (MRTO4) is a member of the ribosomal protein L10P family. MRTO4 is a protein sharing a low level of sequence similarity with ribosomal protein P0. Though the precise function of the MRTO4 is presently unknown, it seems to be involved in mRNA turnover and ribosome assembly. MRTO4 is a nucleolar component of the ribosome assembly apparatus which shares remarkable similarity and contends for binding to the 25S rRNA GAR domain with the ribosomal protein P0. The MRTO4 gene is located on human chromosome 1, which extends over 260 million base pairs, is comprised of over 3,000 genes and contains approximately 8% of the human genome.

    • Synonyms

      MRNA Turnover 4 Homolog (S. Cerevisiae), MRT4 MRNA Turnover 4 Homolog (S. Cerevisiae), 60S Acidic Ribosomal Protein PO, Chromosome 1 Open Reading Frame 33, C1orf33, MRT4, DJ657E11.4.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMPKSKRD KKVSLTKTAK KGLELKQNLI EELRKCVDTY KYLFIFSVAN MRNSKLKDIR NAWKHSRMFF GKNKVMMVAL GRSPSDEYKD NLHQVSKRLR GEVGLLFTNR TKEEVNEWFT KYTEMDYARA GNKAAFTVSL DPGPLEQFPH SMEPQLRQLG LPTALKRGVV TLLSDYEVCK EGDVLTPEQA RVLKLFGYEM AEFKVTIKYM WDSQSGRFQQ MGDDLPESAS ESTEESDSED DD

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mrto4 Human
  • View Data Sheet

    Name :

    BCDIN3D Human

    Description:

    BCDIN3D Human Recombinant

    Pre-miRNA 5'-monophosphate methyltransferase, BCDIN3 domain-containing protein, BCDIN3D.

    Product # :

    PRO-1262

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    Description

    BCDIN3D Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292 a.a) and having a molecular mass of 35kDa.BCDIN3D is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BCDIN3D protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol, 1mM DTT and 2mM EDTA.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BCDIN3D is a member of the methyltransferase superfamily and contains 1 Bin3-type SAM domain. BCDIN3D acts in the catalysis of the transfer of a methyl group to an acceptor molecule. BCDIN3D is an O-methyltransferase which specifically dimethylates the 5' monophosphate of pre-miRNAs, serving as a negative regulator of miRNA processing. BCDIN3D mediates the methylation of pre-miR-145, as well as other pre-miRNAs.

    • Synonyms

      Pre-miRNA 5'-monophosphate methyltransferase, BCDIN3 domain-containing protein, BCDIN3D.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAVPTEL DGGSVKETAA EEESRVLAPG AAPFGNFPHY SRFHPPEQRL RLLPPELLRQ LFPESPENGP ILGLDVGCNS GDLSVALYKH FLSLPDGETC SDASREFRLL CCDIDPVLVK RAEKECPFPD ALTFITLDFM NQRTRKVLLS SFLSQFGRSV FDIGFCMSIT MWIHLNHGDH GLWEFLAHLS SLCHYLLVEP QPWKCYRAAA RRLRKLGLHD FDHFHSLAIR GDMPNQIVQI LTQDHGMELI CCFGNTSWDR SLLLFRAKQT IETHPIPESL IEKGKEKNRL SFQKQ.

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    Bcdin3D Human
  • View Data Sheet

    Name :

    GDNF Rat

    Description:

    Glial-Derived Neurotrophic Factor Rat Recombinant

    ATF1, ATF2, HFB1-GDNF, GDNF.

    Product # :

    CYT-403

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    Description

    Glial derived Neurotrophic Factor Rat Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 134 amino acids and having a total molecular mass of 29.8 kDa.

    Source

    Escherichia Coli.

    Formulation

    GDNF was lyophilized from a sterile solution containing 1xPBS, pH 7.4.

    Purity

    Greater than 98.0% as determined by HPLC analysis and by SDS-PAGE.

    Biological Activity

    Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

    More Info

    • Introduction

      GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
      GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.

    • Synonyms

      ATF1, ATF2, HFB1-GDNF, GDNF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Glial-derived Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDNF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Glial Derived Neurotrophic Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI

    • Background

      What is the molecular weight/Mw of GDNF RAT Protein?
      GDNF RAT Protein has a total Mw of 29.8kDa.

      What is the source or expression system of GDNF RAT Protein?
      Escherichia Coli.

      What is the Purity of GDNF RAT Protein?
      GDNF RAT Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDNF RAT Protein?
      Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

      What is the amino acid sequence of GDNF RAT Protein?
      SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI

      What applications can GDNF RAT Protein be used in?
      GDNF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDNF RAT Protein?
      The endotoxin level is minimal, GDNF RAT Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Gdnf Rat
  • View Data Sheet

    Name :

    CEBP Gamma Human

    Description:

    CCAAT/enhancer binding protein C/EBP Gamma Recombinant Human

    CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.

    Product # :

    PRO-434

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    Description

    CEBP-g Recombinant Human His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 146 (aa 39-147) and having a molecular mass of 16.5 kDa. The DNA binding domain of CEBP-g was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCAAT/enhancer binding protein(C/EBP) g is a family of transcription factors all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and/or form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBP g may cooperate with Fos to bind PRE- enhancer elements.

    • Synonyms

      CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMPGG GGKAVAPSKQ SKKSSPMDRN SDEYRQRRER NNMAVKKSRL KSKQKAQDTL QRVNQLKEEN ERLEAKIKLL TKELSVLKDL FLEHAHNLAD NVQSISTENT TADGDN.

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    Cebpg Human
  • View Data Sheet

    Name :

    MIP 1a Human

    Description:

    Macrophage Inflammatory Protein-1 Alpha Human Recombinant (CCL3)

    Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.

    Product # :

    CHM-233

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    Description

    Macrophage Inflammatory Protein-1 alpha Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from 0.55 mg/ml solution containing no additives.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophilsand basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.

    • Synonyms

      Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Macrophage Inflammatory Protein-1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Ser-Leu-Ala-Ala.

    • Background

      What is the molecular weight/Mw of MIP 1A HUMAN Protein?
      MIP 1A HUMAN Protein has a total Mw of 7.82kDa.

      What is the source or expression system of MIP 1A HUMAN Protein?
      Escherichia Coli.

      What is the Purity of MIP 1A HUMAN Protein?
      MIP 1A HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of MIP 1A HUMAN Protein?
      The Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of MIP 1A HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Ser-Leu-Ala-Ala.

      What applications can MIP 1A HUMAN Protein be used in?
      MIP 1A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for MIP 1A HUMAN Protein?
      The endotoxin level is minimal, MIP 1A HUMAN Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mip 1A Human
  • View Data Sheet

    Name :

    SNX3 Human

    Description:

    Sorting Nexin 3 Human Recombinant

    Sorting nexin-3, Protein SDP3, SNX3, SDP3, Grd19, MCOPS8.

    Product # :

    PRO-246

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    Description

    SNX3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-162 a.a) and having a molecular mass of 20.9kDa.SNX3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SNX3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sorting nexin 3 (SNX3) belongs to the large family of hydrophilic proteins, which interact with various receptor types and are involved in intracellular trafficking. SNX3 interacts with phosphatidylinositol-3-phosphate, and is involved in protein trafficking. SNX3 comprises a distinct subgroup of nexins, which share less sequence similarity outside of the PX domain and have significantly different binding affinities for the tyrosine kinase receptors.

    • Synonyms

      Sorting nexin-3, Protein SDP3, SNX3, SDP3, Grd19, MCOPS8.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      SNX3 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAETVADTRR LITKPQNLND AYGPPSNFLE IDVSNPQTVG VGRGRFTTYE IRVKTNLPIF KLKESTVRRR YSDFEWLRSE LERESKVVVP PLPGKAFLRQ LPFRGDDGIF DDNFIEERKQ GLEQFINKVA GHPLAQNERC LHMFLQDEII DKSYTPSKIR
      HA.

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    Snx3 Human
  • View Data Sheet

    Name :

    MBP Antibody

    Description:

    Maltose-Binding protein, Mouse Antibody

    MBP, Maltose-Binding protein.

    Product # :

    ANT-451

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, 10% glycerol & 0.02% Sodium Azide.

    More Info

    • Introduction

      Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes. MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

    • Synonyms

      MBP, Maltose-Binding protein.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti MBP mAb is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant MBP purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P10C12AT.

    • Applications

      MBP antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Antibody Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      MBP antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Anti Mbp
  • View Data Sheet

    Name :

    GNAI3 Human

    Description:

    Guanine Nucleotide Binding Protein Alpha Inhibiting Activity 3 Human Recombinant

    Guanine nucleotide binding protein (G protein) alpha inhibiting activity polypeptide 3, G(i) alpha-3, 87U6.

    Product # :

    PRO-1074

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    GNAI3 Human Recombinant produced in E. coli is a single polypeptide chain containing 377 amino acids (1-354) and having a molecular mass of 43.0kDa.GNAI3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GNAI3 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNAI3 is a member of the G-alpha family and G (i/o/t/z) subfamily which act as modulators or transducers in several transmembrane signaling systems. G(k) is the stimulatory G protein of receptor-regulated K+ channels. The active GTP-bound form inhibits the connotation of RGS14 with centrosomes and is essential for the translocation of RGS14 from the cytoplasm to the plasma membrane. GNAI3 takes part in cell division and is known to cooperate with RIC8A, S1PR1, RGS5, RGS10, RGS12, RGS14, RGS16, RGS18, and RGS19.

    • Synonyms

      Guanine nucleotide binding protein (G protein) alpha inhibiting activity polypeptide 3, G(i) alpha-3, 87U6.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMGCTLSA EDKAAVERSK MIDRNLREDG EKAAKEVKLL LLGAGESGKS TIVKQMKIIH EDGYSEDECK QYKVVVYSNT IQSIIAIIRA MGRLKIDFGE AARADDARQL FVLAGSAEEG VMTPELAGVI KRLWRDGGVQ ACFSRSREYQ LNDSASYYLN DLDRISQSNY IPTQQDVLRT RVKTTGIVET HFTFKDLYFK MFDVGGQRSE RKKWIHCFEG VTAIIFCVAL SDYDLVLAED EEMNRMHESM KLFDSICNNK WFTETSIILF LNKKDLFEEK IKRSPLTICY PEYTGSNTYE EAAAYIQCQF EDLNRRKDTK EIYTHFTCAT DTKNVQFVFD AVTDVIIKNN LKECGLY

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Gnai3 Human
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